@article{ref1,
title="A pore forming peptide from spider Lachesana sp. venom induced neuronal depolarization and pain",
journal="Biochimica et biophysica acta",
year="2014",
author="Okada, Masayoshi and Corzo, Gerardo and Romero-Perez, Gustavo A. and Coronas, Fredy I. V. and Matsuda, Hiroko and Possani, Lourival D.",
volume="1850",
number="4",
pages="657-666",
abstract="BACKGROUND: Arachnoid venoms contain numerous peptides with ion channel modifying and cytolytic activities. <br><br>METHODS: We developed a green fluorescent protein (GFP)-based assay that can monitor the changes in currents through overexpressed inwardly rectifying K(+) channels (Kir2.1), in which GFP expression was increased by blockade of Kir2.1 current. Using this assay, we screened venom of many spider species. A peptide causing GFP decreasing effect was purified and sequenced. Electrophysiological and pain-inducing effects of the peptide were analyzed with whole-cell patch-clamp recordings and hot-plate test, respectively. <br><br>RESULTS: Among venoms we screened, soluble venom from Lachesana sp decreased the GFP expression. Purification and sequencing of the peptide showed that the peptide is identical to a pore-forming peptide purified from Lachesana tarabaevi venom. Whole cell patch-clamp recordings revealed that the peptide had no effect on Kir2.1 current. Instead, it induced a current that was attributable to the pore-formation of the peptide. The peptide was selectively incorporated into hyperpolarized, i.e., Kir2.1 expressing, cells and for this reason the peptide decreased GFP expression in our Kir2.1 assay. The pore-formation positively shifted the reversal potential and induced burst firings in the hippocampal neurons in a synaptic current-independent way. The application of the Lachesana sp peptide induced pain-related behavior in mice, CONCLUSIONS: The peptide, which was found in Lachesana sp venom, formed pores and thereby depolarized neurons and induced pain. GENERAL SIGNIFICANCE: Our data suggested an additional physiological role of the pore-forming peptides.<p /> <p>Language: en</p>",
language="en",
issn="0006-3002",
doi="10.1016/j.bbagen.2014.11.022",
url="http://dx.doi.org/10.1016/j.bbagen.2014.11.022"
}